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MASA Protein Crystal

(CBCRY26)  Download Datasheet
Background
Background
Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively.
Molecular Description
Protein Classification
Hydrolase
Structure Weight
29316.11 Da
Polymer
1
Molecule
E-1 Enzyme
Chain Length
285 amino acids
Crystal Description
PDB ID
1ZS9
MMDB ID
33918
Source
E.coli
Method
X-Ray Diffraction
Resolution
1.7Å
Ligand Chemical Component
Selenomethionine
Gene Information
Gene Name
ENOPH1
Synonyms
DKFZp586M0524; E1; FLJ12594; MASA; MST145; E-1 enzyme; Enolase-phosphatase E1; MSTP145 protein; acireductone synthase; EC 3.1.3.77; 2,3-diketo-5-methylthio-1-phosphopentane phosphatase; MASA homolog
UniProt ID
Q9UHY7
Gene ID
58478
Chromosome Location
4q21.22
Function
magnesium ion binding; phosphor-glycolate phosphatase activity; acireductone synthase activity; metal ion binding; catalytic activity
Reference
Reference
Wang, H., Pang, H., Bartlam, M., Rao, Z. (2005) Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase J.Mol.Biol. 348: 917-926